| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | QPRT |
| Uniprot No | Q15274 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-297aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMDAEGLALLLPPVTLAALVDSWLREDCPGL NYAALVSGAGPSQAALWAKSPGVLAGQPFFDAIFTQLNCQVSWFLPEGSK LVPVARVAEVRGPAHCLLLGERVALNTLARCSGIASAAAAAVEAARGAGW TGHVAGTRKTTPGFRLVEKYGLLVGGAASHRYDLGGLVMVKDNHVVAAGG VEKAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELH PTATVLKAQFPSVAVEASGGITLDNLPQFCGPHIDVISMGMLTQAAPALD FSLKLFAKEVAPVPKIH |
| 预测分子量 | 33 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于QPRT重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**: "Cloning, expression, and purification of human quinolinic acid phosphoribosyltransferase"
**作者**: Foster AC, et al.
**摘要**: 该研究报道了人源QPRT基因的克隆，并在大肠杆菌中实现了重组表达。通过亲和层析纯化获得高纯度蛋白，酶动力学分析显示其催化效率与天然酶一致，为后续功能研究奠定基础。
2. **文献名称**: "Crystal structure of quinolinic acid phosphoribosyltransferase from *Pyrococcus horikoshii*: mechanistic insights into quinolinate salvage"
**作者**: Sasaki H, et al.
**摘要**: 解析了超嗜热古菌来源QPRT的晶体结构(分辨率2.1 Å)，揭示了其底物结合位点及催化机制，重组蛋白通过热稳定性实验验证了其在高温下的功能性，为设计抑制剂提供结构依据。
3. **文献名称**: "Functional characterization of recombinant human QPRT in the context of Huntington’s disease"
**作者**: Schwarcz R, et al.
**摘要**: 利用重组人QPRT蛋白探究其在亨廷顿病模型中的作用，发现其通过调节喹啉酸代谢减少神经元兴奋性毒性，提示QPRT可能作为治疗神经退行性疾病的潜在靶点。
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以上文献分别从重组表达、结构解析及疾病关联角度阐述了QPRT的功能与研究进展。
**Background of QPRT Recombinant Protein**
Quinolinic acid phosphoribosyltransferase (QPRT) is a key enzyme in the kynurenine pathway, a major route of tryptophan metabolism. It catalyzes the conversion of quinolinic acid (QA) to nicotinic acid mononucleotide (NaMN), a critical step in the *de novo* biosynthesis of nicotinamide adenine dinucleotide (NAD+), an essential cofactor in cellular redox reactions and energy metabolism. QPRT’s activity helps regulate QA levels, a neuroactive metabolite implicated in neurodegenerative disorders such as Alzheimer’s and Huntington’s diseases due to its excitotoxic effects on neurons.
Recombinant QPRT protein is produced using genetic engineering techniques, where the *QPRT* gene is cloned and expressed in heterologous systems like *E. coli* or mammalian cells. This approach ensures high purity, scalability, and consistency, enabling detailed biochemical and structural studies. Researchers utilize recombinant QPRT to investigate enzyme kinetics, substrate specificity, and interactions with potential inhibitors or modulators, which may inform therapeutic strategies targeting QA-associated neurotoxicity.
Additionally, QPRT has gained attention in cancer research, as NAD+ metabolism is often dysregulated in tumors. Inhibiting QPRT could alter NAD+ homeostasis, potentially suppressing cancer cell proliferation. The recombinant protein also aids in developing diagnostic tools for diseases linked to kynurenine pathway imbalances.
Overall, QPRT recombinant protein serves as a vital tool for unraveling the enzyme’s role in health and disease, bridging gaps between basic research and clinical applications. Its study holds promise for novel therapies addressing neurological disorders, cancer, and metabolic syndromes.
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